摘要
高丝氨酸内脂合成酶(homoserine lactone synthase,abaI)是导致鲍曼不动杆菌生物被膜形成的关键酶之一,对其结构功能的研究有助于我们对抑制生物被膜形成有很大帮助。本研究通过Genebank查找abaI(A1S_0109)蛋白序列,运用分子技术对其进行表达分析,应用生物分析软件ExPASy、ESPript、MEG5.0、SWISS-MODEL等对其进行结构分析,使用分子对接软件分析抑制剂的关键结合位点。结果显示,在含有pET28a-abaI重组质粒BL21菌株与野生BL21菌株相比生物被膜形成能力以及运动性显著增高。从生成生物膜被膜的定义上,BL21从不产生物被膜菌株,变成了产膜菌株。预测其结构蛋白与TofI蛋白高度相似,通过分子对接首次揭示abaI蛋白抑制剂与abaI蛋白相互作用关系。研究结果显示abaI在BL21中能够促使生物被膜的形成和增强细菌的运动,分子对接揭示了abaI蛋白的相互作用位点,为进一步研究其活性以及抑制剂提供了重要的参考信息。
Homoserine lactone synthase(abaI)is one of the key enzymes leading to the biofilm formation of Acinetobacter baumannii.Studying the structure and function of abaI is helpful for us to inhibit biofilm formation.In this study,the sequence of abaI(a1 s_0109)protein was found by Genebank.The expression of abaI was analyzed by molecular technology.The structure of abaI was analyzed by using biological analysis software ExPASY,espript,MEG5.0 and SWISS-MODEL.Key binding sites of inhibitors were analyzed using molecular docking software.The results of biofilm formation test showed that the biofilm formation ability and motility of BL21-abaI strain was significantly higher than that of wild BL21 strain.In terms of the definition of biofilm formation,BL21 strain never produced biofilm,became a weak biofilm producing strain.The transformation of abaI in BL21 can promote the formation of biofilm and enhance the movement of bacteria.It is predicted that structure of abaI is highly similar to TofI protein.Molecular docking revealed the interaction between abaI protein inhibition and abaI protein for the first time.The results show that abaI can promote the biofilm formation and motility in BL21.Molecular docking reveals the interaction sites of abaI protein,which provides important reference information for the further study of its activity and inhibitors.
作者
乔霞
苏雅静
康宇婷
汪澎涛
贾伟
QIAO Xia;SU Ya-jing;KANG Yu-ting;WANG Peng-tao;JIA Wei(Ningxia Key Laboratory of Clinical and Pathogenic Microbiology,General Hospital of Ningxia Medical University,Yinchuan 750004,China;Center of Laboratory Medicine,General Hospital of Ningxia Medical University,Yinchuan 750004,China)
出处
《化学研究与应用》
CAS
CSCD
北大核心
2022年第12期2886-2893,共8页
Chemical Research and Application
基金
本项目研究由宁夏自然科学基金项目(2019AAC03223)资助。
